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Figure 3.
Binding of InsP[6] increases pro-CPD/C-S T[m], and the
protein becomes trypsin-resistant.A, close-up view of InsP[6]
binding pocket shows 12 residues known to contact InsP[6] (red
with space-filling dots) derive from the N terminus (blue), the
protease core (green), and the β-flap (magenta). B, SYPRO®
Orange melting curves of pro-CPD/C-S at different concentrations
of InsP[6]. C, Coomassie-stained gel of limited proteolysis of
pro-CPD/C-S at varying concentrations of trypsin. Locations of
trypsin cleavage in the absence of InsP[6] as determine by FT-MS
(supplemental Fig. 4) are shown in orange in D with color scheme
used in A except antiparallel β8β9 are highlighted pink and S1
hydrophobic residues are space-filling dots.
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